Obtaining and Purifying the Recombinant Domain III of Human Alpha-Fetoprotein

Previous studies have demonstrated the applicability of alpha-fetoprotein or its receptor-binding domain fused to the 6-histidine tag at the C-terminus (rAFP3D-His6) as vectors for targeted delivery of antitumor agents. The His6 tag is undesirable for further preclinical trials. Therefore, we design...

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Veröffentlicht in:	Applied biochemistry and microbiology 2022-12, Vol.58 (8), p.899-908
Hauptverfasser:	Yabbarov, N. G., Mollaev, M. D., Zabolotskii, A. I., Mazalev, D. A., Gorokhovets, N. V., Sokol, M. B., Mollaeva, M. R., Fomicheva, M. V., Pshenichnikova, A. B., Nikolskaya, E. D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acid sequence Ammonium sulfate Anticancer properties Antitumor agents Biochemistry Biology Biomedical and Life Sciences C-Terminus Cellulose Circular dichroism Clinical trials Dichroism Domains Drug delivery E coli Gene Engineering Histidine Hydrophobicity Inclusion bodies Life Sciences Mass spectrometry Mass spectroscopy Medical Microbiology Microbiology Nucleotide sequence Producers Protein folding Protein purification Protein structure Proteins Purification Secondary structure Selection Tumor cells α-Fetoprotein
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